This project involves a detailed study of the mechanisms which regulate the dismutation reaction in the mitochondria of the parasitic helminth, Ascaris suum. The project also entails a study of the interaction of the glycolytic enzyme aldolase with the muscle protein, actin, A procedure will be developed to purify fumarase from the muscle tissue of the roundworm. The purified fumarase will then be subjected to physico-chemical and kinetic studies. Correlation of the kinetic properties of fumarase will be made with the same parameters of malic enzyme in an attempt to discover subtle control mechanisms in the energy production of the parasite. Studies on the heterologous protein associations of aldolase and actin will involve proteolytic enzymes as probes to changes in structure of the proteins when they interact. BIBLIOGRAPHIC REFERENCES: Supowit, S. and Harris, B. 1976. Ascaris suum hexokinase: purification and possible function in compartmentation of glucose 6-phosphate in muscle. Biochim. Biophys. Acta 422, 48-59. Landsperger, W. and Harris, B. 1976. NAD ion-malic enzyme: regulatory properties of the enzyme from Ascaris suum. J. Biol. Chem. (In Press).